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Effect of chain chirality on the self-assembly of sickle hemoglobin

Xuejin Li1, Bruce Caswell, George Em Karniadakis

  • 1Division of Applied Mathematics, Brown University, Providence, Rhode Island, USA.

Biophysical Journal
|September 22, 2012
PubMed

We present simulation results on the self-assembly behavior of sickle hemoglobin (HbS). A coarse-grained HbS model, which contains hydrophilic and hydrophobic particles explicitly, is constructed to match the structural properties and physical description of HbS. The hydrophobic interactions are shown to be necessary with chirality being the main driver for the formation of HbS fibers. In the absence of chain chirality, only small self-assembled aggregates are observed whereas self-assembled elongated steplike bundle microstructures appear when we include chain chirality. We also investigate the effect of confinement on self-assembly, and find that elongated fibers-similar to open-space ones-can be obtained in hard confinement domains but cannot be formed within compliant red blood cell (RBC) domains under the same assumptions. We show, however, that by placing explicitly HbS fibers inside the RBCs and subjecting them to linear elongation and bending, we obtain different types of sickle-shaped RBCs as observed in sickle cell anemia.

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